Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Antigenicity of Partial Fragments of Recombinant Pasteurella multocida Toxin

  • Lee, Jeong-Min (Research Institute for Veterinary Science, College of Veterinary Medicine, Seoul National University) ;
  • Woo, Hee-Jong (Research Institute for Veterinary Science, College of Veterinary Medicine, Seoul National University)
  • Received : 2010.04.22
  • Accepted : 2010.08.16
  • Published : 2010.12.28
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Abstract

Pasteurella multocida serogroup D strain, which produces P. multocida toxin (PMT), is a widespread and harmful pathogen of respiratory diseases such as pneumonia and progressive atrophic rhinitis (PAR) in swine. Vaccination has been considered the most desirable and effective approach for controlling the diseases caused by toxigenic P. multocida. To investigate the antigenicity and immunogenicity of partial fragments of recombinant PMT, recombinant proteins of the N-terminal (PMT-A), middle (PMT-B), C-terminal (PMT-C), and middle-C-terminal (PMT2.3) regions of PMT were successfully produced in an Escherichia coli expression system. The molecular masses of PMT-A, PMT-B, PMT-C, and PMT2.3 were ca. 53, 55, 35, and 84 kDa, respectively, purified by nickel-nitrilotriacetic acid (Ni-NTA) affinity column chromatography. All the recombinant proteins except for PMT-A showed immune responses to antisera obtained from a swine showing symptoms of PAR. Moreover, high titers of PMT-specific antibodies were raised from mice immunized with each of the recombinant proteins; however, the immunoreactivities of the antibodies to authentic PMT and heat-inactivated whole bacteria were different, respectively. In the protection study, the highest protection against homologous challenge was shown in the case of PMT2.3; relatively poor protections occurred for the other PMT fragments.

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References

  1. Adler, B., D. Bulach, J. Chung, S. Doughty, M. Hunt, K. Rajakumar, et al. 1999. Candidate vaccine antigens and genes in Pasteurella multocida. J. Biotechnol. 73: 83-90. https://doi.org/10.1016/S0168-1656(99)00111-X
  2. Bagley, K. C., S. F. Abdelwahab, R. G. Tuskan, and G. K. Lewis. 2005. Pasteurella multocida toxin activates human monocyte-derived and murine bone marrow-derived dendritic cells in vitro but suppresses antibody production in vivo. Infect. Immun. 73: 413-421. https://doi.org/10.1128/IAI.73.1.413-421.2005
  3. Baldwin, M. R., J. H. Lakey, and A. J. Lax. 2004. Identification and characterization of the Pasteurella multocida toxin translocation domain. Mol. Microbiol. 54: 239-250. https://doi.org/10.1111/j.1365-2958.2004.04264.x
  4. Brown, W. F. 1964. Variance estimation in the Reed-Muench fifty per cent end-point determination. Am. J. Hyg. 79: 37-46.
  5. Busch, C., J. Orth, N. Djouder, and K. Aktories. 2001. Biological activity of a C-terminal fragment of Pasteurella multocida toxin. Infect. Immun. 69: 3628-3634. https://doi.org/10.1128/IAI.69.6.3628-3634.2001
  6. Carter, G. R. 1955. Studies on Pasteurella multocida. I. A hemagglutination test for the identification of serological types. Am. J. Vet. Res. 16: 481-484.
  7. Dabo, S. M., A. W. Confer, and G. L. Murphy. 1997. Outer membrane proteins of bovine Pasteurella multocida serogroup A isolates. Vet. Microbiol. 54: 167-183. https://doi.org/10.1016/S0378-1135(96)01274-6
  8. Felix, R., H. Fleisch, and P. L. Frandsen. 1992. Effect of Pasteurella multocida toxin on bone resorption in vitro. Infect. Immun. 60: 4984-4988.
  9. Foged, N. T. 1992. Pasteurella multocida toxin. The characterisation of the toxin and its significance in the diagnosis and prevention of progressive atrophic rhinitis in pigs. APMIS Suppl. 25: 1-56.
  10. Foged, N. T., J. P. Nielsen, and S. E. Jorsal. 1989. Protection against progressive atrophic rhinitis by vaccination with Pasteurella multocida toxin purified by monoclonal antibodies. Vet. Rec. 125: 7-11. https://doi.org/10.1136/vr.125.1.7
  11. Foged, N. T., J. P. Nielsen, and K. B. Pedersen. 1988. Differentiation of toxigenic from nontoxigenic isolates of Pasteurella multocida by enzyme-linked immunosorbent assay. J. Clin. Microbiol. 26: 1419-1420.
  12. Harper, M., J. D. Boyce, and B. Adler. 2006. Pasteurella multocida pathogenesis: 125 years after Pasteur. FEMS Microbiol. Lett. 265: 1-10. https://doi.org/10.1111/j.1574-6968.2006.00442.x
  13. Heddleston, K. L., J. E. Gallagher, and P. A. Rebers. 1972. Fowl cholera: Gel diffusion precipitin test for serotyping Pasteurella multocida from avian species. Avian Dis. 16: 925-936. https://doi.org/10.2307/1588773
  14. Kitadokoro, K., S. Kamitani, M. Miyazawa, M. Hanajima-Ozawa, A. Fukui, M. Miyake, and Y. Horiguchi. 2007. Crystal structures reveal a thiol protease-like catalytic triad in the Cterminal region of Pasteurella multocida toxin. Proc. Natl. Acad. Sci. U.S.A. 104: 5139-5144. https://doi.org/10.1073/pnas.0608197104
  15. Lax, A. J. and N. Chanter. 1990. Cloning of the toxin gene from Pasteurella multocida and its role in atrophic rhinitis. J. Gen. Microbiol. 136: 81-87. https://doi.org/10.1099/00221287-136-1-81
  16. Lee, J., S. Kang, S. I. Park, H. J. Woo, and M. Kwon. 2004. Molecular cloning and characterization of the gene for outer membrane protein H in a Pasteurella multocida (D:4) isolate from pigs with atrophic rhinitis symptoms in Korea. J. Microbiol. Biotechnol. 14: 1343-1349.
  17. Lee, J., Y. B. Kim, and M. Kwon. 2007. Outer membrane protein H for protective immunity against Pasteurella multocida. J. Microbiol. 45: 179-184.
  18. Liao, C. M., C. Huang, S. L. Hsuan, Z. W. Chen, W. C. Lee, C. I. Liu, J. R. Winton, and M. S. Chien. 2006. Immunogenicity and efficacy of three recombinant subunit Pasteurella multocida toxin vaccines against progressive atrophic rhinitis in pigs. Vaccine 24: 27-35. https://doi.org/10.1016/j.vaccine.2005.07.079
  19. Mullan, P. B. and A. J. Lax. 1998. Pasteurella multocida toxin stimulates bone resorption by osteoclasts via interaction with osteoblasts. Calcif. Tissue Int. 63: 340-345. https://doi.org/10.1007/s002239900537
  20. Nakai, T., A. Sawata, M. Tsuji, Y. Samejima, and K. Kume. 1984. Purification of dermonecrotic toxin from a sonic extract of Pasteurella multocida SP-72 serotype D. Infect. Immun. 46: 429-434.
  21. Petersen, S. K., N. T. Foged, A. Bording, J. P. Nielsen, H. K. Riemann, and P. L. Frandsen. 1991. Recombinant derivatives of Pasteurella multocida toxin: Candidates for a vaccine against progressive atrophic rhinitis. Infect. Immun. 59: 1387-1393.
  22. Pullinger, G. D., R. Sowdhamini, and A. J. Lax. 2001. Localization of functional domains of the mitogenic toxin of Pasteurella multocida. Infect. Immun. 69: 7839-7850. https://doi.org/10.1128/IAI.69.12.7839-7850.2001
  23. Rajeev, S., R. V. Nair, S. A. Kania, and D. A. Bemis. 2003. Expression of a truncated Pasteurella multocida toxin antigen in Bordetella bronchiseptica. Vet. Microbiol. 94: 313-323. https://doi.org/10.1016/S0378-1135(03)00137-8
  24. Register, K. B., R. E. Sacco, and S. L. Brockmeier. 2007. Immune response in mice and swine to DNA vaccines derived from the Pasteurella multocida toxin gene. Vaccine 25: 6118-6128. https://doi.org/10.1016/j.vaccine.2007.05.028
  25. Rhoades, K. R. and R. B. Rimler. 1987. Effects of Pasteurella multocida endotoxins on turkey poults. Avian Dis. 31: 523-526. https://doi.org/10.2307/1590734
  26. Rhoades, K. R. and R. B. Rimler. 1990. Virulence and toxigenicity of capsular serogroup D Pasteurella multocida strains isolated from avian hosts. Avian Dis. 34: 384-388. https://doi.org/10.2307/1591424
  27. Rimler, R. B., R. D. Angus, and M. Phillips. 1989. Evaluation of the specificity of Pasteurella multocida somatic antigen-typing antisera prepared in chickens, using ribosome-lipopolysaccharide complexes as inocula. Am. J. Vet. Res. 50: 29-31.
  28. Sakano, T., M. Okada, A. Taneda, T. Mukai, and S. Sato. 1997. Effect of Bordetella bronchiseptica and serotype D Pasteurella multocida bacterin-toxoid on the occurrence of atrophic rhinitis after experimental infection with B. bronchiseptica and toxigenic type A P. multocida. J. Vet. Med. Sci. 59: 55-57. https://doi.org/10.1292/jvms.59.55
  29. Seo, J., H. Pyo, S. Lee, J. Lee, and T. Kim. 2009. Expression of 4 truncated fragments of Pasteurella multocida toxin and their immunogenicity. Can. J. Vet. Res. 73: 184-189.
  30. Tabatabaei, M., Z. Liu, A. Finucane, R. Parton, and J. Coote. 2002. Protective immunity conferred by attenuated aroA derivatives of Pasteurella multocida B:2 strains in a mouse model of hemorrhagic septicemia. Infect. Immun. 70: 3355-3362. https://doi.org/10.1128/IAI.70.7.3355-3362.2002
  31. To, H., S. Someno, and S. Nagai. 2005. Development of a genetically modified nontoxigenic Pasteurella multocida toxin as a candidate for use in vaccines against progressive atrophic rhinitis in pigs. Am. J. Vet. Res. 66: 113-118. https://doi.org/10.2460/ajvr.2005.66.113
  32. van Diemen, P. M., G. de Vries Reilingh, and H. K. Parmentier. 1994. Immune responses of piglets to Pasteurella multocida toxin and toxoid. Vet. Immunol. Immunopathol. 41: 307-321. https://doi.org/10.1016/0165-2427(94)90104-X
  33. Vasfi Marandi, M. and K. R. Mittal. 1997. Role of outer membrane protein H (OmpH)- and OmpA-specific monoclonal antibodies from hybridoma tumors in protection of mice against Pasteurella multocida. Infect. Immun. 65: 4502-4508.
  34. Wilson, B. A., V. G. Ponferrada, J. E. Vallance, and M. Ho. 1999. Localization of the intracellular activity domain of Pasteurella multocida toxin to the N terminus. Infect. Immun. 67: 80-87.

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